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Q63716 (PRDX1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxiredoxin-1

EC=1.11.1.15
Alternative name(s):
HBP23
Heme-binding 23 kDa protein
Thioredoxin peroxidase 2
Thioredoxin-dependent peroxide reductase 2
Gene names
Name:Prdx1
Synonyms:Tdpx2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation By similarity.

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Subunit structure

Homodimer; disulfide-linked, upon oxidation. May form heterodimers with AOP2. Interacts with GDPD5; forms a mixed-disulfide with GDPD5 By similarity.

Subcellular location

Cytoplasm. Melanosome By similarity.

Post-translational modification

Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity By similarity.

Miscellaneous

The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin.

Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized.

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRedox-active center
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from electronic annotation. Source: Compara

erythrocyte homeostasis

Inferred from electronic annotation. Source: Compara

hydrogen peroxide catabolic process

Inferred from electronic annotation. Source: Compara

natural killer cell mediated cytotoxicity

Inferred from electronic annotation. Source: Compara

regulation of NF-kappaB import into nucleus

Inferred from electronic annotation. Source: Compara

regulation of stress-activated MAPK cascade

Inferred from electronic annotation. Source: Compara

removal of superoxide radicals

Inferred from electronic annotation. Source: Compara

response to oxidative stress

Inferred from direct assay PubMed 17556052. Source: RGD

   Cellular_componentcytosol

Inferred from direct assay PubMed 11350800PubMed 7488219Ref.1. Source: RGD

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial matrix

Inferred from direct assay PubMed 14623930. Source: RGD

nuclear euchromatin

Inferred from direct assay PubMed 14623930. Source: RGD

nucleolus

Inferred from direct assay PubMed 14623930. Source: RGD

peroxisomal matrix

Inferred from direct assay PubMed 14623930. Source: RGD

   Molecular_functionheme binding

Inferred from physical interaction Ref.1. Source: RGD

peroxiredoxin activity

Inferred from direct assay PubMed 11350800PubMed 7488219. Source: RGD

protein homodimerization activity

Inferred from direct assay Ref.4. Source: RGD

thioredoxin peroxidase activity

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 199198Peroxiredoxin-1
PRO_0000135078

Regions

Domain6 – 165160Thioredoxin

Sites

Active site521Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue71N6-acetyllysine By similarity
Modified residue161N6-acetyllysine By similarity
Modified residue271N6-acetyllysine By similarity
Modified residue351N6-acetyllysine By similarity
Modified residue901Phosphothreonine By similarity
Disulfide bond52Interchain (with C-173); in linked form
Disulfide bond173Interchain (with C-52); in linked form

Secondary structure

..................................... 199
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q63716 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BDF2D4ABA8A776DA

FASTA19922,109
        10         20         30         40         50         60 
MSSGNAKIGH PAPSFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS 

        70         80         90        100        110        120 
DRAEEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK 

       130        140        150        160        170        180 
ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDEILRLV QAFQFTDKHG EVCPAGWKPG 

       190 
SDTIKPDVNK SKEYFSKQK 

« Hide

References

« Hide 'large scale' references
[1]"Purification, characterization, and cloning of a heme-binding protein (23 kDa) in rat liver cytosol."
Iwahara S., Satoh H., Song D.-X., Webb J., Burlingame A.L., Nagae Y., Mueller-Eberhard U.
Biochemistry 34:13398-13406(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver and Pituitary.
[3]Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 17-35 AND 111-190, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
[4]"Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product."
Hirotsu S., Abe Y., Okada K., Nagahara N., Hori H., Nishino T., Hakoshima T.
Proc. Natl. Acad. Sci. U.S.A. 96:12333-12338(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN OXIDIZED FORM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D30035 mRNA. Translation: BAA06275.1.
BC058450 mRNA. Translation: AAH58450.1.
BC088118 mRNA. Translation: AAH88118.1.
IPIIPI00211779.
PIRI52425.
RefSeqNP_476455.1. NM_057114.1.
UniGeneRn.2845.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QQ2X-ray2.60A/B1-199[»]
2Z9SX-ray2.90A/B/C/D/E/F/G/H/I/J1-199[»]
ProteinModelPortalQ63716.
SMRQ63716. Positions 3-199.
ModBaseSearch...

Protein-protein interaction databases

IntActQ63716. 3 interactions.
STRING10116.ENSRNOP00000023132.

Protein family/group databases

PeroxiBase4508. Rno2CysPrx01.

PTM databases

PhosphoSiteQ63716.

2D gel databases

World-2DPAGE0004:Q63716.

Proteomic databases

PaxDbQ63716.
PRIDEQ63716.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000023132; ENSRNOP00000023132; ENSRNOG00000017194.
GeneID117254.
KEGGrno:117254.
UCSCRGD:620039. rat.

Organism-specific databases

CTD5052.
RGD620039. Prdx1.

Phylogenomic databases

eggNOGCOG0450.
GeneTreeENSGT00390000004653.
HOGENOMHOG000022343.
HOVERGENHBG000286.
InParanoidQ63716.
KOK13279.
OMATISTDYG.
OrthoDBEOG4V6ZHJ.

Gene expression databases

GenevestigatorQ63716.
GermOnlineENSRNOG00000017194. Rattus norvegicus.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ63716.
NextBio620108.

Entry information

Entry namePRDX1_RAT
AccessionPrimary (citable) accession number: Q63716
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families